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| | ==Crystal structure of the FhaA FHA domain complexed with the intracellular domain of Rv3910== | | ==Crystal structure of the FhaA FHA domain complexed with the intracellular domain of Rv3910== |
| - | <StructureSection load='3oun' size='340' side='right' caption='[[3oun]], [[Resolution|resolution]] 2.71Å' scene=''> | + | <StructureSection load='3oun' size='340' side='right'caption='[[3oun]], [[Resolution|resolution]] 2.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3oun]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OUN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3oun]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OUN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.705Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3otv|3otv]], [[3ouk|3ouk]], [[3uqc|3uqc]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oun OCA], [https://pdbe.org/3oun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oun RCSB], [https://www.ebi.ac.uk/pdbsum/3oun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oun ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0020c, TB39.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]), MT4029, Rv3910 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oun RCSB], [http://www.ebi.ac.uk/pdbsum/3oun PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/P71590_MYCTU P71590_MYCTU]] Regulates cell growth and peptidoglycan synthesis by binding to MviN. May inhibit the late stages of peptidoglycan synthesis.<ref>PMID:22275220</ref> [[http://www.uniprot.org/uniprot/O05435_MYCTU O05435_MYCTU]] Essential for cell growth and peptidoglycan synthesis. | + | [https://www.uniprot.org/uniprot/FHAA_MYCTU FHAA_MYCTU] Regulates cell growth and peptidoglycan synthesis by binding to MviN. May inhibit the late stages of peptidoglycan synthesis.<ref>PMID:22275220</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3oun" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Mycobacterium tuberculosis]] | + | [[Category: Large Structures]] |
| - | [[Category: Alber, T]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Gee, C L]] | + | [[Category: Alber T]] |
| - | [[Category: Fha domain]] | + | [[Category: Gee CL]] |
| - | [[Category: Membrane associated intracellular]]
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| - | [[Category: Peptidoglycan]]
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| - | [[Category: Phosphorylation]]
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| - | [[Category: Protein binding-transferase complex]]
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| - | [[Category: Pseudokinase]]
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| - | [[Category: Regulation]]
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| - | [[Category: Ser/thr kinase]]
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| Structural highlights
Function
FHAA_MYCTU Regulates cell growth and peptidoglycan synthesis by binding to MviN. May inhibit the late stages of peptidoglycan synthesis.[1]
Publication Abstract from PubMed
Prokaryotic cell wall biosynthesis is coordinated with cell growth and division, but the mechanisms regulating this dynamic process remain obscure. Here, we describe a phosphorylation-dependent regulatory complex that controls peptidoglycan (PG) biosynthesis in Mycobacterium tuberculosis. We found that PknB, a PG-responsive Ser-Thr protein kinase (STPK), initiates complex assembly by phosphorylating a kinase-like domain in the essential PG biosynthetic protein, MviN. This domain was structurally diverged from active kinases and did not mediate phosphotransfer. Threonine phosphorylation of the pseudokinase domain recruited the FhaA protein through its forkhead-associated (FHA) domain. The crystal structure of this phosphorylated pseudokinase-FHA domain complex revealed the basis of FHA domain recognition, which included unexpected contacts distal to the phosphorylated threonine. Conditional degradation of these proteins in mycobacteria demonstrated that MviN was essential for growth and PG biosynthesis and that FhaA regulated these processes at the cell poles and septum. Controlling this spatially localized PG regulatory complex is only one of several cellular roles ascribed to PknB, suggesting that the capacity to coordinate signaling across multiple processes is an important feature conserved between eukaryotic and prokaryotic STPK networks.
A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria.,Gee CL, Papavinasasundaram KG, Blair SR, Baer CE, Falick AM, King DS, Griffin JE, Venghatakrishnan H, Zukauskas A, Wei JR, Dhiman RK, Crick DC, Rubin EJ, Sassetti CM, Alber T Sci Signal. 2012 Jan 24;5(208):ra7. PMID:22275220[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gee CL, Papavinasasundaram KG, Blair SR, Baer CE, Falick AM, King DS, Griffin JE, Venghatakrishnan H, Zukauskas A, Wei JR, Dhiman RK, Crick DC, Rubin EJ, Sassetti CM, Alber T. A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria. Sci Signal. 2012 Jan 24;5(208):ra7. PMID:22275220 doi:10.1126/scisignal.2002525
- ↑ Gee CL, Papavinasasundaram KG, Blair SR, Baer CE, Falick AM, King DS, Griffin JE, Venghatakrishnan H, Zukauskas A, Wei JR, Dhiman RK, Crick DC, Rubin EJ, Sassetti CM, Alber T. A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria. Sci Signal. 2012 Jan 24;5(208):ra7. PMID:22275220 doi:10.1126/scisignal.2002525
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